Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Henrik Fridén"'
Publikováno v:
Biochemistry. 34:11080-11089
The membrane-anchoring subunit of Bacillus subtilis succinate:menaquinone reductase is a protein of 202 residues containing two protoheme IX groups with bis-histidine axial ligation. Residues Kis13, His28, His70, His113, and His155 are the possible h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2d13f062ef2ee8e7a1160a2abe552000
https://doi.org/10.1021/bi00035a013
https://doi.org/10.1021/bi00035a013
Publikováno v:
Molecular Microbiology. 4:1881-1889
Summary The decay of the polycistronic Bacillus subtilis sdh mRNA was analysed using probes specific for each of the component cistrons, sdhC, sdhA and sdhB. In exponentially growing cells, the entire sdh mRNA seems to decay with an ‘all or nothing
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c3171c68528cf6ecb54fa1b3fbf863bb
https://doi.org/10.1111/j.1365-2958.1990.tb02037.x
https://doi.org/10.1111/j.1365-2958.1990.tb02037.x
Publikováno v:
Dynamics of Membrane Assembly ISBN: 9783662028629
Translocating a protein across a membrane, or getting one assembled into it, is one of the most complex—yet routine—activities that cells are called upon to perform. It is a form of transport that transports transporters, uses receptors to assemb
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::656e9c68d2a38cde19d746b9f0adff13
https://doi.org/10.1007/978-3-662-02860-5_17
https://doi.org/10.1007/978-3-662-02860-5_17
Autor:
Lars Hederstedt, Myles R. Cheesman, Andrew J. Thomson, Kristoffer K. Andersson, Henrik Fridén
Publikováno v:
Biochimica et biophysica acta. 1041(2)
Bacillus subtilis cytochrome b-558 was expressed in high amounts in Escherichia coli, solubilized from membranes with detergent and purified free from other hemoproteins. The cytochrome possibly contains two heme groups. To determine the axial ligand
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4954160aedce6464b3bc5572766784dd
https://pubmed.ncbi.nlm.nih.gov/2176107
https://pubmed.ncbi.nlm.nih.gov/2176107
Publikováno v:
FEMS Microbiology Letters. 41:203-206
Plasmid pKIM2 carries the Bacillus subtilis sdh operon and adjacent regions of the bacterial chromosome. The plasmid replicates in Escherichia coli but not in B. subtilis. Different portions of the sdh operon were removed from pKIM2 and replaced by a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ec5bc93c4cf045c978d75d5555d7ceff
https://doi.org/10.1111/j.1574-6968.1987.tb02197.x
https://doi.org/10.1111/j.1574-6968.1987.tb02197.x
Publikováno v:
Scopus-Elsevier
Bacillus subtilis succinate dehydrogenase is bound to the cytoplasmic membrane by cytochrome b-558, a 23-kDa transmembrane protein which also functions as electron acceptor to the dehydrogenase. The structural gene for the apocytochrome, sdhC, has pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::909a179a717fc469340ca73a15d947cd
https://doi.org/10.1111/j.1432-1033.1987.tb13471.x
https://doi.org/10.1111/j.1432-1033.1987.tb13471.x
Autor:
Henrik Fridén, Lars Hederstedt
Publikováno v:
Cytochrome Systems ISBN: 9781461290780
The membranebound tricarboxylic acid cycle enzyme succinate dehydrogenase (SDH) is associated with a b-type cytochrome in many organisms. 1,2 The cytochrome b is often found in stoichiometric amounts in isolated succinate-ubiquinone oxidoreductase (c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6ad4e15f43b5bd9d3b19a90430270d5b
https://doi.org/10.1007/978-1-4613-1941-2_88
https://doi.org/10.1007/978-1-4613-1941-2_88
Autor:
Lars Hederstedt, Henrik Fridén
Publikováno v:
Scopus-Elsevier
Cytochrome b558 in the cytoplasmic membrane of Bacillus subtilis constitutes the anchor and electron acceptor to the flavoprotein (Fp) and iron-sulphur protein (Ip) in succinate:quinone oxidoreductase, and seemingly contains two haem groups. EPR and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::46a273cacb67258ccf8043498bd45b67
http://www.scopus.com/inward/record.url?eid=2-s2.0-0025286626&partnerID=MN8TOARS
http://www.scopus.com/inward/record.url?eid=2-s2.0-0025286626&partnerID=MN8TOARS